Zinc in PDB 1v0d: Crystal Structure of Caspase-Activated Dnase (Cad)

The structure of Crystal Structure of Caspase-Activated Dnase (Cad), PDB code: 1v0d was solved by E.-J.Woo, Y.-G.Kim, M.-S.Kim, W.-D.Han, S.Shin, B.-H.Oh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30 / 2.6
Space group	P 64
Cell size a, b, c (Å), α, β, γ (°)	110.189, 110.189, 73.982, 90.00, 90.00, 120.00
R / Rfree (%)	21.8 / 24.6

The structure of Crystal Structure of Caspase-Activated Dnase (Cad) also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Lead	(Pb)	1 atom

The binding sites of Zinc atom in the Crystal Structure of Caspase-Activated Dnase (Cad) (pdb code 1v0d). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Caspase-Activated Dnase (Cad), PDB code: 1v0d:

Zinc binding site 1 out of 1 in the Crystal Structure of Caspase-Activated Dnase (Cad)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Caspase-Activated Dnase (Cad) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:50.2 occ:1.00 SG A:CYS307 2.2 49.2 1.0 ND1 A:HIS242 2.2 47.6 1.0 SG A:CYS238 2.3 58.9 1.0 SG A:CYS229 2.4 45.8 1.0 CE1 A:HIS242 3.0 47.2 1.0 CB A:CYS229 3.1 46.4 1.0 CB A:CYS307 3.3 52.3 1.0 CG A:HIS242 3.3 47.7 1.0 CB A:CYS238 3.3 61.6 1.0 CB A:HIS242 3.8 48.8 1.0 CB A:HIS304 4.1 53.0 1.0 NE2 A:HIS242 4.1 48.4 1.0 CA A:CYS238 4.2 62.0 1.0 CD2 A:HIS242 4.3 47.2 1.0 CA A:GLY231 4.3 52.0 1.0 N A:GLY231 4.4 53.7 1.0 N A:HIS242 4.5 53.4 1.0 CA A:CYS229 4.6 50.0 1.0 CA A:CYS307 4.6 53.0 1.0 N A:HIS304 4.7 51.3 1.0 N A:CYS307 4.7 51.8 1.0 CA A:HIS242 4.8 51.2 1.0 CG A:HIS304 4.9 54.1 1.0 CB A:SER240 4.9 57.1 1.0 C A:CYS229 4.9 52.3 1.0 C A:CYS238 5.0 61.5 1.0

E.-J.Woo, Y.-G.Kim, M.-S.Kim, W.-D.Han, S.Shin, H.Robinson, S.-Y.Park, B.-H.Oh. Structural Mechanism For Inactivation and Activation of Cad/DFF40 in the Apoptotic Pathway Mol.Cell V. 14 531 2004.
ISSN: ISSN 1097-2765
PubMed: 15149602
DOI: 10.1016/S1097-2765(04)00258-8